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- PDB-2w2c: STRUCTURE OF THE TETRADECAMERIC OLIGOMERISATION DOMAIN OF CALCIUM... -

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Basic information

Entry
Database: PDB / ID: 2w2c
TitleSTRUCTURE OF THE TETRADECAMERIC OLIGOMERISATION DOMAIN OF CALCIUM- CALMODULIN DEPENDENT PROTEIN KINASE II DELTA
ComponentsCALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
KeywordsTRANSFERASE / SERINE/THREONINE-PROTEIN KINASE / KINASE / ATP-BINDING / PHOSPHOPROTEIN / CALMODULIN-BINDING / NUCLEOTIDE-BINDING
Function / homology
Function and homology information


regulation of relaxation of cardiac muscle / regulation of cellular localization / negative regulation of sodium ion transmembrane transport / regulation of cardiac muscle cell action potential involved in regulation of contraction / calcium- and calmodulin-dependent protein kinase complex / regulation of cell communication by electrical coupling / : / Ca2+/calmodulin-dependent protein kinase / regulation of membrane depolarization / regulation of the force of heart contraction ...regulation of relaxation of cardiac muscle / regulation of cellular localization / negative regulation of sodium ion transmembrane transport / regulation of cardiac muscle cell action potential involved in regulation of contraction / calcium- and calmodulin-dependent protein kinase complex / regulation of cell communication by electrical coupling / : / Ca2+/calmodulin-dependent protein kinase / regulation of membrane depolarization / regulation of the force of heart contraction / Trafficking of AMPA receptors / endoplasmic reticulum calcium ion homeostasis / cardiac muscle cell contraction / sodium channel inhibitor activity / calcium/calmodulin-dependent protein kinase activity / Assembly and cell surface presentation of NMDA receptors / regulation of calcium ion transmembrane transport via high voltage-gated calcium channel / relaxation of cardiac muscle / CaMK IV-mediated phosphorylation of CREB / regulation of cardiac muscle cell action potential / regulation of heart contraction / regulation of cell communication by electrical coupling involved in cardiac conduction / positive regulation of cardiac muscle hypertrophy / Phase 0 - rapid depolarisation / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / regulation of heart rate by cardiac conduction / Ion transport by P-type ATPases / regulation of neuronal synaptic plasticity / Long-term potentiation / Regulation of MECP2 expression and activity / regulation of ryanodine-sensitive calcium-release channel activity / HSF1-dependent transactivation / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of protein localization to plasma membrane / positive regulation of cardiac muscle cell apoptotic process / Ion homeostasis / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / titin binding / sarcoplasmic reticulum membrane / peptidyl-threonine phosphorylation / Ras activation upon Ca2+ influx through NMDA receptor / cellular response to calcium ion / regulation of cell growth / RAF activation / sarcolemma / long-term synaptic potentiation / Interferon gamma signaling / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / endocytic vesicle membrane / peptidyl-serine phosphorylation / RAF/MAP kinase cascade / protein autophosphorylation / transmembrane transporter binding / calmodulin binding / neuron projection / postsynaptic density / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / regulation of transcription by RNA polymerase II / protein homodimerization activity / nucleoplasm / ATP binding / identical protein binding / nucleus / membrane / cytosol / cytoplasm
Similarity search - Function
Calcium/calmodulin-dependent protein kinase II, association-domain / Calcium/calmodulin dependent protein kinase II association domain / Nuclear Transport Factor 2; Chain: A, - #50 / NTF2-like domain superfamily / Nuclear Transport Factor 2; Chain: A, / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Roll ...Calcium/calmodulin-dependent protein kinase II, association-domain / Calcium/calmodulin dependent protein kinase II association domain / Nuclear Transport Factor 2; Chain: A, - #50 / NTF2-like domain superfamily / Nuclear Transport Factor 2; Chain: A, / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Roll / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / : / Calcium/calmodulin-dependent protein kinase type II subunit delta
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsPike, A.C.W. / Rellos, P. / Sethi, R. / Salah, E. / Burgess-Brown, N. / Shrestha, L. / Roos, A. / Murray, J.W. / von Delft, F. / Edwards, A. ...Pike, A.C.W. / Rellos, P. / Sethi, R. / Salah, E. / Burgess-Brown, N. / Shrestha, L. / Roos, A. / Murray, J.W. / von Delft, F. / Edwards, A. / Arrowsmith, C.H. / Weigelt, J. / Bountra, C. / Knapp, S.
CitationJournal: Plos Biol. / Year: 2010
Title: Structure of the Camkiidelta/Calmodulin Complex Reveals the Molecular Mechanism of Camkii Kinase Activation.
Authors: Rellos, P. / Pike, A.C.W. / Niesen, F.H. / Salah, E. / Lee, W.H. / von Delft, F. / Knapp, S.
History
DepositionOct 28, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 23, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Aug 10, 2011Group: Database references / Derived calculations / Refinement description
Revision 1.3Dec 20, 2017Group: Database references / Structure summary / Category: audit_author / citation_author / Item: _audit_author.name / _citation_author.name
Revision 1.4Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
B: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
C: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
D: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
E: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
F: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
G: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
H: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
I: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
J: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
K: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
L: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
M: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
N: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)231,30334
Polymers229,80214
Non-polymers1,50120
Water1,67593
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area34340 Å2
ΔGint-224.4 kcal/mol
Surface area76090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)149.546, 117.803, 160.761
Angle α, β, γ (deg.)90.00, 111.92, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21D
31E
41F
51G
61H
71I
81J
91K
101L
111N
12B
22C
32M

NCS domain segments:

Refine code: 1

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111VALVALALAALAAA343 - 40212 - 71
211VALVALALAALADD343 - 40212 - 71
311VALVALALAALAEE343 - 40212 - 71
411VALVALALAALAFF343 - 40212 - 71
511VALVALALAALAGG343 - 40212 - 71
611VALVALALAALAHH343 - 40212 - 71
711VALVALALAALAII343 - 40212 - 71
811VALVALALAALAJJ343 - 40212 - 71
911VALVALALAALAKK343 - 40212 - 71
1011VALVALALAALALL343 - 40212 - 71
1111VALVALALAALANN343 - 40212 - 71
121PROPROGLYGLYAA409 - 47178 - 140
221PROPROGLYGLYDD409 - 47178 - 140
321PROPROGLYGLYEE409 - 47178 - 140
421PROPROGLYGLYFF409 - 47178 - 140
521PROPROGLYGLYGG409 - 47178 - 140
621PROPROGLYGLYHH409 - 47178 - 140
721PROPROGLYGLYII409 - 47178 - 140
821PROPROGLYGLYJJ409 - 47178 - 140
921PROPROGLYGLYKK409 - 47178 - 140
1021PROPROGLYGLYLL409 - 47178 - 140
1121PROPROGLYGLYNN409 - 47178 - 140
112VALVALALAALABB343 - 40212 - 71
212VALVALALAALACC343 - 40212 - 71
312VALVALALAALAMM343 - 40212 - 71
122PROPROGLYGLYBB409 - 47178 - 140
222PROPROGLYGLYCC409 - 47178 - 140
322PROPROGLYGLYMM409 - 47178 - 140

NCS ensembles :
ID
1
2

NCS oper:
IDCodeMatrixVector
1given(0.7916, 0.5866, -0.1711), (-0.5834, 0.6421, -0.4973), (-0.1819, 0.4935, 0.8505)-19.84, 15.22, -16.87
2given(0.1844, 0.03081, 0.9824), (-0.006621, -0.9994, 0.03258), (0.9828, -0.01251, -0.1841)-61.56, 69.51, 73.36
3given(0.2991, 0.7453, -0.5959), (-0.7485, -0.2041, -0.631), (-0.5919, 0.6347, 0.4968)-23.92, 45.16, -20.28
4given(-0.9395, 0.3386, 0.05218), (0.3395, 0.9001, 0.273), (0.04548, 0.2742, -0.9606)-71.19, 3.25, 65.84
5given(0.7566, -0.6271, -0.1853), (0.6225, 0.6039, 0.4978), (-0.2003, -0.492, 0.8473)23.16, 13.88, 17.45
6given(-0.114, 0.3524, -0.9289), (-0.3235, -0.8972, -0.3007), (-0.9393, 0.2662, 0.2162)-9.131, 69, -7.691
7given(0.2345, -0.7563, -0.6108), (0.7526, -0.2565, 0.6065), (-0.6153, -0.6019, 0.509)28.86, 44.59, 21.42
8given(-0.1313, -0.3184, -0.9388), (0.3311, -0.9067, 0.2612), (-0.9344, -0.2766, 0.2245)14.47, 67.65, 11.12
9given(-0.9342, -0.3526, 0.05505), (-0.353, 0.8907, -0.2863), (0.0519, -0.2869, -0.9566)-45.48, 4.558, 85.76
10given(-0.4887, -0.7754, 0.3998), (-0.7717, 0.1705, -0.6127), (0.407, -0.608, -0.6817)-29.36, 31.1, 96.86
11given(-0.01471, -0.5892, 0.8078), (-0.6021, -0.6398, -0.4777), (0.7983, -0.4934, -0.3453)-38.65, 59.02, 91.13
12given(-0.05365, 0.6156, 0.7862), (0.6012, -0.6087, 0.5177), (0.7973, 0.5005, -0.3375)-81.86, 55.11, 56.39
13given(-0.5685, 0.74, 0.3595), (0.7284, 0.2497, 0.638), (0.3823, 0.6245, -0.681)-85.27, 24.46, 52.93

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Components

#1: Protein
CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA CHAIN / CALCIUM CAMOLDULIN DEPENDENT KINASE 2D


Mass: 16414.443 Da / Num. of mol.: 14 / Fragment: OLIGOMERISATION DOMAIN, RESIDUES 334-475
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PNIC28-BSA4 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): R3-PRARE2
References: UniProt: Q13557, Ca2+/calmodulin-dependent protein kinase
#2: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C2H3O2
#3: Chemical
ChemComp-CD / CADMIUM ION


Mass: 112.411 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Cd
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 93 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.86 Å3/Da / Density % sol: 57 % / Description: NONE
Crystal growpH: 4.6
Details: 30% PEG400, 0.1M CADMIUM CHLORIDE, 0.1M SODIUM ACETATE PH4.6

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.97888
DetectorType: MARRESEARCH / Detector: CCD / Date: Jul 24, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97888 Å / Relative weight: 1
ReflectionResolution: 2.7→44.86 Å / Num. obs: 323492 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Biso Wilson estimate: 84.77 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 11.6
Reflection shellResolution: 2.7→2.85 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.76 / Mean I/σ(I) obs: 2.3 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.5.0055refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 1HKX,2UX0,2F86

1hkx

2ux0

2f86


Resolution: 2.7→44.8 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.916 / SU B: 24.45 / SU ML: 0.225 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.619 / ESU R Free: 0.303 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES RESIDUAL ONLY. A BOUND ACETATE ION HAS BEEN MODELLED IN EACH MONOMER HOWEVER THE DIFFERENCE DENSITY SUGGESTS THAT THE TRUE BOUND ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES RESIDUAL ONLY. A BOUND ACETATE ION HAS BEEN MODELLED IN EACH MONOMER HOWEVER THE DIFFERENCE DENSITY SUGGESTS THAT THE TRUE BOUND MOIETY IS A LARGER CARBOXYLATE CONTAINING ENTITY. STRONG DIFFERENCE DENSITY BETWEEN SYMMETRY-RELATED OLIGOMERIC RINGS HAS BEEN MODELLED BY PARTIALLY-OCCUPIED CADMIUM IONS WHICH WERE PRESENT IN THE CRYSTALLIZATION SOLUTION.
RfactorNum. reflection% reflectionSelection details
Rfree0.245 2134 3 %RANDOM
Rwork0.211 ---
obs0.212 68546 99.5 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 36.44 Å2
Baniso -1Baniso -2Baniso -3
1--1.22 Å20 Å2-1.9 Å2
2---2.28 Å20 Å2
3---2.08 Å2
Refinement stepCycle: LAST / Resolution: 2.7→44.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13912 0 62 93 14067
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.02114290
X-RAY DIFFRACTIONr_bond_other_d0.0020.029184
X-RAY DIFFRACTIONr_angle_refined_deg1.3621.91819397
X-RAY DIFFRACTIONr_angle_other_deg0.898322274
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.4851759
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.30424.193737
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.463152135
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.6931581
X-RAY DIFFRACTIONr_chiral_restr0.080.22094
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02116307
X-RAY DIFFRACTIONr_gen_planes_other0.0030.022994
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6081.58893
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.198214162
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.08235397
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.5084.55235
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1556tight positional0.040.05
12D1556tight positional0.040.05
13E1556tight positional0.040.05
14F1556tight positional0.030.05
15G1556tight positional0.030.05
16H1556tight positional0.040.05
17I1556tight positional0.040.05
18J1556tight positional0.030.05
19K1556tight positional0.040.05
110L1556tight positional0.040.05
111N1556tight positional0.030.05
21B1598tight positional0.050.05
22C1598tight positional0.040.05
23M1598tight positional0.040.05
11A1556tight thermal1.845
12D1556tight thermal1.825
13E1556tight thermal1.65
14F1556tight thermal1.55
15G1556tight thermal1.145
16H1556tight thermal1.165
17I1556tight thermal1.25
18J1556tight thermal1.435
19K1556tight thermal1.675
110L1556tight thermal1.955
111N1556tight thermal1.615
21B1598tight thermal1.485
22C1598tight thermal1.625
23M1598tight thermal2.155
LS refinement shellResolution: 2.7→2.77 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.369 176
Rwork0.377 4950
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
15.82051.41730.4344.4545-0.26064.3508-0.24290.44470.3185-0.50940.03480.0792-0.38240.01930.20810.15630.01010.00040.09220.0260.043-42.543263.951112.6764
23.6650.22930.4044.3511-0.55214.29960.03570.581-0.0292-0.44650.06460.03020.1588-0.028-0.10040.0849-0.0280.03820.1561-0.04070.0564-51.777832.63864.6694
34.2473-0.85890.83854.122-0.53885.87830.0731-0.122-0.33260.34870.07010.53290.1309-0.5968-0.14320.07-0.03070.07550.19850.03940.145-55.97747.129930.0281
42.3457-0.69170.07064.951-1.36095.26150.19440.2298-0.4104-0.3743-0.09890.00990.45710.2024-0.09550.11710.04640.00880.0973-0.04880.1163-38.99083.59215.4671
54.9044-1.4330.23354.2869-0.41253.6292-0.0935-0.70330.14280.8637-0.142-0.0082-0.4031-0.07590.23550.2943-0.06270.01490.20020.00160.0517-8.524349.712169.0274
65.0127-0.62140.30133.0232-0.26155.1166-0.02070.53410.4533-0.2039-0.1053-0.3165-0.42310.32480.1260.1799-0.0323-0.04220.10750.08820.2036-17.553773.464633.0343
74.23290.8156-0.3172.91570.88964.56170.14350.2657-0.4357-0.13680.1111-0.60230.58550.5074-0.25460.17420.1222-0.07550.1272-0.05760.3195-13.7753-1.748236.7319
84.8186-1.79690.02626.6483-0.50444.3855-0.00370.28620.2042-0.0076-0.3379-0.6312-0.33310.6430.34150.0802-0.09090.01250.22130.13320.20133.250954.180450.7229
93.8513-0.05670.22424.93411.22695.39090.15930.31-0.07320.10780.0085-0.9204-0.060.6302-0.16780.01650.0123-0.00440.1797-0.07340.45494.635221.157952.9381
105.5296-0.22350.31022.5454-0.2794.5847-0.0678-0.45640.34170.6409-0.02870.2682-0.4806-0.20150.09650.3313-0.00590.00990.0974-0.09870.1614-27.993772.335352.9332
115.16361.43510.14845.63730.51594.1634-0.0331-0.47790.3280.3104-0.18530.4708-0.4515-0.56450.21840.1810.08160.0940.2158-0.0830.1564-53.23466.476332.2959
124.14020.5754-0.48225.5484-0.92255.15910.1948-0.370.17870.34240.07460.4104-0.1416-0.8634-0.26930.05060.03230.06010.29040.0490.0778-65.428237.832622.0234
134.82-0.36520.75452.78340.33454.06960.2701-0.4789-0.55670.5008-0.03210.14890.5616-0.3773-0.23810.2986-0.1019-0.05040.09660.08720.2119-31.653-2.547550.4661
142.7661-0.55180.06664.62680.66873.35880.1637-0.4747-0.06790.8944-0.0507-0.01980.3792-0.2787-0.11290.2946-0.0362-0.0290.15390.03630.206-10.790215.794367.6527
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A339 - 471
2X-RAY DIFFRACTION2B340 - 471
3X-RAY DIFFRACTION3C341 - 471
4X-RAY DIFFRACTION4D342 - 471
5X-RAY DIFFRACTION5E338 - 471
6X-RAY DIFFRACTION6F341 - 471
7X-RAY DIFFRACTION7G341 - 471
8X-RAY DIFFRACTION8H339 - 471
9X-RAY DIFFRACTION9I338 - 471
10X-RAY DIFFRACTION10J342 - 471
11X-RAY DIFFRACTION11K342 - 471
12X-RAY DIFFRACTION12L340 - 471
13X-RAY DIFFRACTION13M343 - 471
14X-RAY DIFFRACTION14N336 - 471

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